Document Detail

Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic studies of proteins.
MedLine Citation:
PMID:  15022197     Owner:  NLM     Status:  MEDLINE    
Solid-state 31P NMR spectroscopy was applied to measure the isotropic chemical shifts, chemical shift anisotropies and asymmetry parameters of three phosphorylated amino acids, O-phospho-L-serine, O-phospho-L-threonine and O-phospho-L-tyrosine. The cross-polarization buildup rates and longitudinal relaxation times of 31P and 1H were-determined and compared with the values measured for a triphosphate (GppCH2p) bound to a crystalline protein (Ras). It is shown that the phosphorylated amino acids are well-suited model compounds, e.g. for the optimization of experiments on crystalline proteins. Two-dimensional exchange experiments on O-phospho-L-tyrosine indicate the existence of an exchange between the two different conformations of the molecule.
Adriana Iuga; Eike Brunner
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Publication Detail:
Type:  Comparative Study; Evaluation Studies; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Magnetic resonance in chemistry : MRC     Volume:  42     ISSN:  0749-1581     ISO Abbreviation:  Magn Reson Chem     Publication Date:  2004 Apr 
Date Detail:
Created Date:  2004-07-02     Completed Date:  2005-03-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9882600     Medline TA:  Magn Reson Chem     Country:  England    
Other Details:
Languages:  eng     Pagination:  369-72     Citation Subset:  IM    
Copyright Information:
2004 John Wiley & Sons, Ltd.
Universität Regensburg, Institut für Biophysik und Physikalische Biochemie, D-93040 Regensburg, Germany.
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MeSH Terms
Amino Acids / analysis*,  chemistry*
Crystallography / methods*
Magnetic Resonance Spectroscopy / methods*
Organophosphorus Compounds / analysis*,  chemistry*
Phosphorus Radioisotopes*
Protein Conformation
Reg. No./Substance:
0/Amino Acids; 0/Organophosphorus Compounds; 0/Phosphorus Radioisotopes; 0/Powders

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